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Allosteric disulphide bonds as reversible mechano-sensitive switches that control protein functions in the vasculature
Disulphide bonds are covalent linkages of two cysteine residues (R-S-S-R′) in proteins. Unlike peptide bonds, disulphide bonds are reversible in nature allowing cleaved bonds to reform. Disulphide bonds are important structural elements that stabilise protein conformation. They can be of catalytic f...
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| 出版年: | Biophys Rev |
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| 主要な著者: | , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
Springer Berlin Heidelberg
2019
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6557944/ https://ncbi.nlm.nih.gov/pubmed/31090016 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1007/s12551-019-00543-0 |
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